Site-directed mutagenesis of Tyr354 in Geobacillus stearothermophilus alanine racemase identifies a role in controlling substrate specificity and a possible role in the evolution of antibiotic resistance

ChemBioChem

Volumn 3, Issue 8, 2002, Pages 789-792

  Patrick, Wayne M ^a   Weisner, Jan ^a   Blackburn, Jonathan M ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Antibiotics; Mutagenesis; Protein evolution; Racemases; Substrate specificity

Indexed keywords

ALANINE RACEMASE; ASPARAGINE; TYROSINE; VANCOMYCIN;

ANTIBIOTIC RESISTANCE; ARTICLE; CATALYSIS; ENTEROCOCCUS GALLINARUM; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; EVOLUTION; GEOBACILLUS STEAROTHERMOPHILUS; MUTATION; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

ALANINE; ALANINE RACEMASE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BACILLACEAE; BINDING SITES; DRUG RESISTANCE, BACTERIAL; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PHOSPHATES; RACEMASES AND EPIMERASES; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; TYROSINE;

BACTERIA (MICROORGANISMS); ENTEROCOCCUS GALLINARUM; GEOBACILLUS STEAROTHERMOPHILUS;

EID: 0036902246     PISSN: 14394227     EISSN: None     Source Type: Journal    
DOI: 10.1002/1439-7633(20020802)3:8<789::AID-CBIC789>3.0.CO;2-D     Document Type: Article

References (13)

1. The thermophilic bacterium previously named Bacillus stearothermophilus has recently been reclassified in the new genus Geobacillus: T. N. Nazina, T. P. Tourova, A. B. Poltaraus, E. V. Novikova, A. A. Grigoryan, A. E. Ivanova, A. M. Lysenko, V. V. Petrunyaka, G. A. Osipov, S. S. Belyaev, M. V. Ivanov, Int. J. Syst. Evol. Microbiol. 2001, 51, 433-446.
2. J. P. Shaw, G. A. Petsko, D. Ringe, Biochemistry 1997, 36, 1329-1342.
3. (a) A. Watanabe, T. Yoshimura, B. Mikami, N. Esaki, J. Biochem. (Tokyo, Jpn.) 1999, 126, 781-786;
4. (b) M. J. Ondrechen, J. M. Briggs, J. A. McCammon, J. Am. Chem. Soc. 2001, 123, 2830-2834.
5. C. G. F. Stamper, A. A. Morollo, D. Ringe, Biochemistry 1998, 37, 10438-10445. The coordinate file is available from the Brookhaven Protein Data Bank, access code 1BD0.
6. Note that primed residues, such as Tyr265′, are contributed to the active site from a different monomer than unprimed residues such as Lys39.
7. (a) K. Hoffmann, E. Schneider-Scherzer, H. Kleinhauf, R. Zocher, J. Biol. Chem. 1994, 269, 12710-12714;
8. (b) T. Nomura, I. Yamamoto, F. Morishita, Y. Furukawa, O. Matsushima, J. Exp. Zool. 2001, 289, 1-9;
9. (c) T. Uo, T. Yoshimura, N. Tanaka, K. Takegawa, N. Esaki, J. Bacteriol. 2001, 183, 2226-2233, and references cited therein.
10. C. A. Arias, M. Martin-Martinez, T. L. Blundell, M. Arthur, P. Courvalin, P. E. Reynolds, Mol. Microbiol. 1999, 31, 1653-1664.
11. W. S. Faraci, C. T. Walsh, Biochemistry 1988, 27, 3267-3276.
12. C. A. Arias, J. Weisner, J. M. Blackburn, P. E. Reynolds, Microbiology 2000, 146, 1727-1734.
13. H. Wolosker, K. N. Sheth, M. Takahashi, J.-P. Mothet, R. O. Brady, Jr., C. D. Ferris, S. H. Snyder, Proc. Natl. Acad. Sci. USA 1999, 96, 721-725.